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Volumn 230, Issue 11, 2005, Pages 787-792

The proteomics of sickle cell disease: Profiling of erythrocyte membrane proteins by 2D-DIGE and tandem mass spectrometry

Author keywords

Proteomics; RBC membrane proteins; Sickle cell disease

Indexed keywords

ACTIN; LIPID; MEMBRANE PROTEIN; OXYGEN RADICAL; PROTEOME;

EID: 28944446014     PISSN: 15353702     EISSN: 15353699     Source Type: Journal    
DOI: 10.1177/153537020523001102     Document Type: Conference Paper
Times cited : (74)

References (27)
  • 1
    • 0000420850 scopus 로고
    • A specific chemical difference between the globins of normal human and sickle-cell anemia haemoglobin
    • Ingram VM. A specific chemical difference between the globins of normal human and sickle-cell anemia haemoglobin. Nature 178:792-794, 1956.
    • (1956) Nature , vol.178 , pp. 792-794
    • Ingram, V.M.1
  • 2
    • 0036255927 scopus 로고    scopus 로고
    • Predictors of outcome in sickle cell disease
    • Quinn CT, Buchanan GR. Predictors of outcome in sickle cell disease. J Pediatr Hematol Oncol 24:244-245, 2002.
    • (2002) J Pediatr Hematol Oncol , vol.24 , pp. 244-245
    • Quinn, C.T.1    Buchanan, G.R.2
  • 3
    • 0035320886 scopus 로고    scopus 로고
    • Phenotype-genotype relationships in monogenic disease: Lessons from the thalassaemias
    • Weatherall DJ. Phenotype-genotype relationships in monogenic disease: lessons from the thalassaemias. Nat Rev Genet 2:245-255, 2001.
    • (2001) Nat Rev Genet , vol.2 , pp. 245-255
    • Weatherall, D.J.1
  • 4
    • 0036177721 scopus 로고    scopus 로고
    • Sickle cell vaso-occlusion: Multistep and multicellular paradigm
    • Frenette PS. Sickle cell vaso-occlusion: multistep and multicellular paradigm. Curr Opin Hematol 9:101-106, 2002.
    • (2002) Curr Opin Hematol , vol.9 , pp. 101-106
    • Frenette, P.S.1
  • 6
    • 2642551423 scopus 로고    scopus 로고
    • The human erythrocyte proteome: Analysis by ion trap tandem mass spectrometry
    • Kakhniashvili DG, Bulla LA Jr., Goodman SR. The human erythrocyte proteome: analysis by ion trap tandem mass spectrometry. Mol Cell Proteomics 3:501-509, 2004.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 501-509
    • Kakhniashvili, D.G.1    Bulla Jr., L.A.2    Goodman, S.R.3
  • 7
    • 0025290039 scopus 로고
    • The identification and sequence of the actin-binding domain of human red cell β-spectrin
    • Karinch AM, Zimmer WE, Goodman SR. The identification and sequence of the actin-binding domain of human red cell β-spectrin. J Biol Chem 65:11833-11840, 1990.
    • (1990) J Biol Chem , vol.65 , pp. 11833-11840
    • Karinch, A.M.1    Zimmer, W.E.2    Goodman, S.R.3
  • 8
    • 0141560824 scopus 로고    scopus 로고
    • Insect resistance to Bacillus thuringiensis: Alterations in the indianmeal moth larval gut proteome
    • Candas M, Loseva O, Oppert B, Kosaraju P, Bulla LA Jr. Insect resistance to Bacillus thuringiensis: alterations in the indianmeal moth larval gut proteome. Mol Cell Proteomics 2:19-28, 2003.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 19-28
    • Candas, M.1    Loseva, O.2    Oppert, B.3    Kosaraju, P.4    Bulla Jr., L.A.5
  • 9
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JR III. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5:976-989, 1994.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 10
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates JR III, Eng JK, McCormack AL, Schieltz D. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal Chem 67:1426-1436, 1995.
    • (1995) Anal Chem , vol.67 , pp. 1426-1436
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 11
    • 0007170020 scopus 로고
    • Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells
    • U S A
    • Conboy JG, Chang J, Mohandas N, Kan YW. Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells. Proc Natl Acad Sci U S A 85:9062-9065, 1988.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 9062-9065
    • Conboy, J.G.1    Chang, J.2    Mohandas, N.3    Kan, Y.W.4
  • 12
    • 0028370512 scopus 로고
    • Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin
    • Kubota H, Hynes G, Carne A, Ashworth A, Willison K. Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin. Curr Biol 4:89-99, 1994.
    • (1994) Curr Biol , vol.4 , pp. 89-99
    • Kubota, H.1    Hynes, G.2    Carne, A.3    Ashworth, A.4    Willison, K.5
  • 13
    • 0001314116 scopus 로고    scopus 로고
    • Structure and function of chaperonins in Archaebacteria and eucaryotic cytosol
    • Ellis RJ, Ed. San Diego: Academic Press
    • Willison KR, Horwich AI. Structure and function of chaperonins in Archaebacteria and eucaryotic cytosol. In: Ellis RJ, Ed. The Chaperonins. San Diego: Academic Press, p107, 1996.
    • (1996) The Chaperonins , pp. 107
    • Willison, K.R.1    Horwich, A.I.2
  • 14
    • 0018159499 scopus 로고
    • Spectrin binding and control of membrane protein mobility
    • Goodman SR, Branton D. Spectrin binding and control of membrane protein mobility. J Supramol Struct 8: 455-463, 1978.
    • (1978) J Supramol Struct , vol.8 , pp. 455-463
    • Goodman, S.R.1    Branton, D.2
  • 15
    • 0019311634 scopus 로고
    • The effect of endogenous proteases on the spectrin binding proteins of human erythrocytes
    • Siegel DL, Goodman SR, Branton D. The effect of endogenous proteases on the spectrin binding proteins of human erythrocytes. Biochim Biophys Acta 598:517-27, 1980.
    • (1980) Biochim Biophys Acta , vol.598 , pp. 517-527
    • Siegel, D.L.1    Goodman, S.R.2    Branton, D.3
  • 18
    • 0031010267 scopus 로고    scopus 로고
    • Flotilin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins
    • Bickel PE, Scherer PE, Schnitzer JE, Oh P, Lisanti MP, Lodish HF. Flotilin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. J Biol Chem 272:13793-13802, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 13793-13802
    • Bickel, P.E.1    Scherer, P.E.2    Schnitzer, J.E.3    Oh, P.4    Lisanti, M.P.5    Lodish, H.F.6
  • 19
    • 0036682475 scopus 로고    scopus 로고
    • Stomatin is a major lipid-raft component of platelet alpha granules
    • Mairhofer M, Steiner M, Mosgoeler W, Prohaska R, Salzer U. Stomatin is a major lipid-raft component of platelet alpha granules. Blood 100:897-904, 2002.
    • (2002) Blood , vol.100 , pp. 897-904
    • Mairhofer, M.1    Steiner, M.2    Mosgoeler, W.3    Prohaska, R.4    Salzer, U.5
  • 22
    • 9644300915 scopus 로고    scopus 로고
    • The proteasome: A proteolytic nanomachine of cell regulation and waste disposal
    • Wolf DH, Hilt W. The proteasome: a proteolytic nanomachine of cell regulation and waste disposal. Biochim Biophys Acta 1695:19-31, 2004.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 19-31
    • Wolf, D.H.1    Hilt, W.2
  • 23
    • 0023682264 scopus 로고
    • Levels of active ubiquitin carrier proteins decline during erythroid maturation
    • Pickart CM, Vella AT. Levels of active ubiquitin carrier proteins decline during erythroid maturation. J Biol Chem 263:12028-12035, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 12028-12035
    • Pickart, C.M.1    Vella, A.T.2
  • 24
    • 0036746499 scopus 로고    scopus 로고
    • Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ionization-time of flight mass spectrometry
    • Low TY, Seow TK, Chung MCM. Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ionization- time of flight mass spectrometry. Proteomics 2:1229-1239, 2002.
    • (2002) Proteomics , vol.2 , pp. 1229-1239
    • Low, T.Y.1    Seow, T.K.2    Chung, M.C.M.3
  • 26
    • 0034045460 scopus 로고    scopus 로고
    • The Gardos channel is responsible for CDNB-induced dense sickle cell formation
    • Shartava A, McIntire J, Shah AK, Goodman SR. The Gardos channel is responsible for CDNB-induced dense sickle cell formation. Am J Hematol 64:184-189, 2000.
    • (2000) Am J Hematol , vol.64 , pp. 184-189
    • Shartava, A.1    McIntire, J.2    Shah, A.K.3    Goodman, S.R.4
  • 27
    • 0025061081 scopus 로고
    • The sickle erythrocyte in double jeopardy: Autooxidation and iron decompartmentalization
    • Hebbel RP. The sickle erythrocyte in double jeopardy: autooxidation and iron decompartmentalization. Semin Hematol 27:51-69, 1990.
    • (1990) Semin Hematol , vol.27 , pp. 51-69
    • Hebbel, R.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.